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Low Protein Adsorption Products and ELISA Related Products
PROTEOSAVE™

Products

PROTEOSAVE™ is a product that blocks nonspecific adsorption of protein, peptide to the inside of a plastic container by the coating of ultra hydrophilic polymer that S-BIO has newly and originally developed.

Features

Reduce the adsorption of proteins, peptides and cells

The unique surface hydroxide group is coating and decreasing the loss of protein sample by preventing non-specific adsorption of protein and peptide.

Improved organic solvents resistance and heat resistance

PROTEOSAVE™ is stable against general used organic solvents, detergents and heating below 100°C.

Applications

Medical Research Institution/Laboratory

Protein Analysis

Adjustment/Preservation

  • To preserve cell expressed proteins and preparation of culture additives and proteins
  • To reduce loss of protein in a valuable sample

Specification

PROTEOSAVE™ (organic solvent resistant and heat resistant)
Cat. NoProductMaterialNoteQty/PkQty/Cs
MS-4205MPROTEOSAVE™
Microtube 0.5mL		PolypropyleneNon-sterilized100500
MS-4255MPROTEOSAVE™
Microtube 0.5mL R
(Sterilized)		PolypropyleneRadiation sterilized100500
MS-4215MPROTEOSAVE™
Microtube 1.5mL		PolypropyleneNon-sterilized100500
MS-4265MPROTEOSAVE™
Microtube 1.5mL R
(Sterized)		PolypropyleneRadiation sterilized100500
MS-4220MPROTEOSAVE™
Microtube 2.0mL		PolypropyleneNon-sterilized100500
MS-4270MPROTEOSAVE™
Microtube 2.0mL R
(Sterized)		PolypropyleneRadiation sterilized100500
MS-4201XPROTEOSAVE™
Slimtube 0.5mL 		PolypropyleneNon-sterilized50500
MS-4202XPROTEOSAVE™
Slimtube 1.5mL		PolypropyleneNon-sterilized50500

Remark

  • Storage: Room temperature
  • Expiration: 2 years after production
PROTEOSAVE™
Cat. NoProductMaterialNoteQty/PkQty/Cs
MS-52150*PROTEOSAVE™
Conicaltube 15mL		Body: PET
Cap: Polyethylene		Non-sterilized5100
MS-52550PROTEOSAVE™
Conicaltube 50mL R
(Sterilized)		Body: Polypropylene
Cap: Polyethylene		Radiation sterilized5100
MS-8296FPROTEOSAVE™
96-wells, Flat Plate		PolystyreneNo Lid,
Non-sterilized		550
MS-8296VPROTEOSAVE™
96-wells, V Plate		PolypropyleneNo Lid,
Non-sterilized		520
MS-82962RPROTEOSAVE™
96-deep wells, V Plate, 2mL		PolypropyleneRadiation sterilized315
MS-8296KPROTEOSAVE™
96-wells, Black, Flat Plate		PolystyreneNo Lid,
Non-sterilized		550
MS-3296UPROTEOSAVE™
96-wells, U Plate		PolystyreneNo Lid,
Non-sterilized		550

Remark

  • Storage: Room temperature
  • Expiration: 2 years after production
  • *: Operational temperature -80ºC to 40ºC

Experiments

Application example in Proteomics Research



Comparison of the number of identified peptides with competitive products

Experimental conditions

Vessl : ProteoSave™SS 1.5mL
Microtube
5 competitive
Sample : Peptides derived from Hep38
Quantity : 300 ng
Method : nanoLC-Ultra 2D with TripleTOF® 5600, AB SCIEX
Column : 75µmx150mm, ChromXP C18-CL, 3µm 120 Å, Ekisigent
Eluent : A: 0.1% FA and 1% ACN
B: 0.1% FA and 99% ACN
Software : Mascot Server
  • Provided by Dr. Masahiro Kamita, Ph.D, National Cancer Center Research Institute, JAPAN.

Application example in analysis of small molecules

Comparison of Non-ionic small compounds with non-coated tube

Experimental conditions

Vessel : PriteoSave™SS 1.5mL Microtube
Non-coated 1.5mL Microtube
Concentration : 0.1 µg/mL
Sample : Non-ionic small molecule
1. Digoxin (Anti-anginal drug)
2. Paclitaxel (Anti-canter drug)
Meadurement : After 1h incubation with non-ionic small molecule, determined the concentration with LC/MS/MS

Adsorption (%) = 100 - Concentration in the 0 and 1h sample / Concentration in the initial sample x 100

  • Provided by SEKISUI MEDICAL CO., LTD., JAPAN

Reference

Proteosave Microtube (Cat. No. MS-4205M,MS-4255M, MS-4215M, MS-4265M, MS-4220M, MS-4270M)

1. YOSHIDA, Mitsutaka, et al. Preferential capture of EpCAM-expressing extracellular vesicles on solid surfaces coated with an aptamer-conjugated zwitterionic polymer. Biotechnology and bioengineering, 2018, 115.3: 536-544.
2. ARISAKA, Yoshinori, et al. A heparin-modified thermoresponsive surface with heparin-binding epidermal growth factor-like growth factor for maintaining hepatic functions in vitro and harvesting hepatocyte sheets. Regenerative Therapy, 2016, 3: 97-106.
3. PANDEY, Kiran; NAHAR, Ashrafun; KADOKAWA, Hiroya. Method for isolating pure bovine gonadotrophs from anterior pituitary using magnetic nanoparticles and anti-gonadotropin-releasing hormone receptor antibody. Journal of Veterinary Medical Science, 2016, 78.11: 1699-1702.
4. HAMAMURA, Kensuke, et al. ANNALS EXPRESS: Simple quantitation for potential serum disease biomarker peptides, primarily identified by a peptidomics approach in the serum with hypertensive disorders of pregnancy. Annals of Clinical Biochemistry: An international journal of biochemistry and laboratory medicine, 2015, 0004563215583697.
5. IZAKI, Shunsuke, et al. Feasibility of Antibody-Poly (Glutamic Acid) Complexes: Preparation of High-Concentration Antibody Formulations and Their Pharmaceutical Properties. Journal of pharmaceutical sciences, 2015, 104.6: 1929-1937.
6. OGISO, Hideo; TANIGUCHI, Makoto; OKAZAKI, Toshiro. Analysis of lipid-composition changes in plasma membrane microdomains. Journal of lipid research, 2015, 56.8: 1594-1605.
7. ICHIKAWA, Shunsuke, et al. Cellulosomal carbohydrate-binding module from Clostridium josui binds to crystalline and non-crystalline cellulose, and soluble polysaccharides. FEBS letters, 2014.
8. KADOKAWA, Hiroya, et al. Gonadotropin-releasing hormone (GnRH) receptors of cattle aggregate on the surface of gonadotrophs and are increased by elevated GnRH concentrations. Animal reproduction science, 2014, 150.3: 84-95.
9. UCHIDA, Yasuo, et al. A study protocol for quantitative targeted absolute proteomics (QTAP) by LC-MS/MS: application for inter-strain differences in protein expression levels of transporters, receptors, claudin-5, and marker proteins at the blood-brain barrier in ddY, FVB, and C57BL/6J mice. Fluids and Barriers of the CNS, 2013, 10.1: 21.
10. NAGAI, Yutaka; TAKAO, Masashi. Monoclonal antibody to human epithelial cell adhesion molecule and method for detecting circulating tumor cells using the same. U.S. Patent Application 14/085,205, 2013.
11. TAKAO, Masashi; NAGAI, Yutaka; TORII, Tokiji. Cysteine-Poor Region-Specific EpCAM Monoclonal Antibody Recognizing Native Tumor Cells with High Sensitivity. Monoclonal antibodies in immunodiagnosis and immunotherapy, 2013, 32.2: 73-80.
12. YASUNO, K., et al. Development of Podocyte Injuries in Osborne-Mendel Rats is Accompanied by Reduced Expression of Podocyte Proteins. Journal of comparative pathology, 2013, 149.2: 280-290.
13. TSUCHIYA, Hikaru; TANAKA, Keiji; SAEKI, Yasushi. The parallel reaction monitoring method contributes to a highly sensitive polyubiquitin chain quantification. Biochemical and biophysical research communications, 2013, 436.2: 223-229.
14. KUROKAWA, Kenji, et al. Novel bacterial lipoprotein structures conserved in low-GC content Gram-positive bacteria are recognized by Toll-like receptor 2. Journal of Biological Chemistry, 2012, 287.16: 13170-13181.
15. UMEMURA, Hiroshi, et al. Identification of a high molecular weight kininogen fragment as a marker for early gastric cancer by serum proteome analysis. Journal of gastroenterology, 2011, 46.5: 577-585.
16. KAWAKAMI, Hirotaka, et al. Dynamics of absolute amount of nephrin in a single podocyte in puromycin aminonucleoside nephrosis rats calculated by quantitative glomerular proteomics approach with selected reaction monitoring mode. Nephrology Dialysis Transplantation, 2011, gfr492.
17. TAKAO, Masashi; TAKEDA, Kazuo. Enumeration, characterization, and collection of intact circulating tumor cells by cross contamination-free flow cytometry. Cytometry Part A, 2011, 79.2: 107-117.
18. FUKUMOTO, Hiroaki, et al. High-molecular-weight β-amyloid oligomers are elevated in cerebrospinal fluid of Alzheimer patients. The FASEB Journal, 2010, 24.8: 2716-2726.
19. ICHIKAWA, S.; KARITA, S. Characterization of Family 3 Carbohydrate-binding Module from Clostridium josui. In: Proceedings of the Second International Workshop on Regional Innovation Studies: (IWRIS2010). Graduate School of Regional Innovation Studies, Mie University, 2010. p. 5-8.

Slim Tube (Cat. No. MS-4201X, MS-4202X)

20. HONJO, Megumi, et al. Autotaxin-lysophosphatidic acid pathway in intraocular pressure regulation and glaucoma subtypes. Investigative ophthalmology & visual science, 2018, 59.2: 693-701.

Conical Tube (Cat. No. MS-52150, MS-52550)

21. MIZUI, Toshiyuki, et al. Cerebrospinal fluid BDNF pro-peptide levels in major depressive disorder and schizophrenia. Journal of psychiatric research, 2019, 113: 190-198.
22. OHARA, Yuki; YOSHIMOTO, Shogo; HORI, Katsutoshi. Control of AtaA-mediated bacterial immobilization by casein hydrolysates. Journal of bioscience and bioengineering, 2019, 128.5: 544-550.
23. ISHII, Takashi, et al. Increased cerebrospinal fluid complement C5 levels in major depressive disorder and schizophrenia. Biochemical and biophysical research communications, 2018, 497.2: 683-688.
24. MATSUMURA, Takayuki, et al. Venom and Antivenom of the Redback Spider (Latrodectus hasseltii) in Japan. Part I. Venom Extraction, Preparation, and Laboratory Testing. Japanese journal of infectious diseases, 2018, 71.2: 116-121.
25. IGARASHI, Nozomi, et al. Increased aqueous autotaxin and lysophosphatidic acid levels are potential prognostic factors after trabeculectomy in different types of glaucoma. Scientific reports, 2018, 8.1: 1-13.
26. HIDESE, Shinsuke, et al. Cerebrospinal fluid neural cell adhesion molecule levels and their correlation with clinical variables in patients with schizophrenia, bipolar disorder, and major depressive disorder. Progress in Neuro-Psychopharmacology and Biological Psychiatry, 2017, 76: 12-18.
27. YOSHIMOTO, Shogo, et al. An Acinetobacter trimeric autotransporter adhesin reaped from cells exhibits its nonspecific stickiness via a highly stable 3D structure. Scientific Reports, 2016, 6.
28. HATTORI, Kotaro, et al. Increased cerebrospinal fluid fibrinogen in major depressive disorder. Scientific reports, 2015, 5: 11412.
29. WATANABE, H., et al. Controlled release of a protein using a ceramic carrier and zinc ions as a novel approach to the treatment of osteoporosis. In: Key Engineering Materials. 2015. p. 332-337.
30. IHARA, Yuta; OHTA, Hiroyuki; MASUDA, Shinji. A highly sensitive quantification method for the accumulation of alarmone ppGpp in Arabidopsis thaliana using UPLC-ESI-qMS/MS. Journal of plant research, 2015, 128.3: 511-518.
31. KIM, Jong-Myong, et al. Highly Reproducible ChIP-on-Chip Analysis to Identify Genome-Wide Protein Binding and Chromatin Status in Arabidopsis thaliana. In: Arabidopsis Protocols. Humana Press, 2014. p. 405-426.

Proteosave 96F Plate (Cat. No. MS-8296F)

32. FURUGORI, Taketoshi; MORISHIMA, Yoshiyuki. PHARMACEUTICAL COMPOSITION FOR PROMOTION OF FIBRINOLYSIS. U.S. Patent Application No 15/538,676, 2017.
33. FUKAZAWA, Tominaga; YAMAZAKI, Yuri; MIYAMOTO, Yohei. Reduction of non-specific adsorption of drugs to plastic containers used in bioassays or analyses. Journal of pharmacological and toxicological methods, 2010, 61.3: 329-333.

Proteosave 96F Plate (Black)(Cat. No. MS-8296K)

34. OBAYASHI, Yumiko; WEI BONG, Chui; SUZUKI, Satoru. Methodological Considerations and Comparisons of Measurement Results for Extracellular Proteolytic Enzyme Activities in Seawater. Frontiers in microbiology, 2017, 8: 1952.
35. ANDOU, Takashi, et al. RNA detection using peptide-inserted Renilla luciferase. Analytical and bioanalytical chemistry, 2009, 393.2: 661-668.

Others

36. SAMESHIMA-YAMASHITA, Yuka, et al. Construction of a Pseudozyma antarctica strain without foreign DNA sequences (self-cloning strain) for high yield production of a biodegradable plastic-degrading enzyme. Bioscience, biotechnology, and biochemistry, 2019, 83.8: 1547-1556.
37. KINOSHITA, Shigeru, et al. Injection of cultured cells with a ROCK inhibitor for bullous keratopathy. New England Journal of Medicine, 2018, 378.11: 995-1003.
38. KOBAYASHI, Jun, et al. Effect of temperature changes on serum protein adsorption on thermoresponsive cell-culture surfaces monitored by a quartz crystal microbalance with dissipation. International journal of molecular sciences, 2018, 19.5: 1516.
39. KUBOTA, Hiroyuki, et al. Reduction in IgE reactivity of Pacific mackerel parvalbumin by heat treatment. Food chemistry, 2016, 206: 78-84.
40. KASUGA, Kie. Comprehensive analysis of MHC ligands in clinical material by immunoaffinity-mass spectrometry. In: The Low Molecular Weight Proteome. Springer New York, 2013. p. 203-218.
41. YAMASHITA, Kazuyuki; SHIROKI, Masahiro. Medical or biochemical resin composition and resin molded product. U.S. Patent Application 13/469,768, 2012.
42. GOTOH, Akiko, et al. Evaluation of adsorption of urine cystatin C to the polymer materials on the microplate by an antigen capture enzyme-linked immunosorbent assay. Clinica Chimica Acta, 2008, 397.1: 13-17.

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